In silico analysis of methyltransferase domains involved in biosynthesis of secondary metabolites.

ABSTRACT:

Background

Secondary metabolites biosynthesized by polyketide synthase (PKS) and nonribosomal peptide synthetase (NRPS) family of enzymes constitute several classes of therapeutically important natural products like erythromycin, rapamycin, cyclosporine etc. In view of their relevance for natural product based drug discovery, identification of novel secondary metabolite natural products by genome mining has been an area of active research. A number of different tailoring enzymes catalyze a variety of chemical modifications to the polyketide or nonribosomal peptide backbone of these secondary metabolites to enhance their structural diversity. Therefore, development of powerful bioinformatics methods for identification of these tailoring enzymes and assignment of their substrate spec

SUBMITTER: Ansari MZ 

PROVIDER: S-EPMC2613160 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature